Relevant bibliographies by topics / DnaB helicase

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'DnaB helicase'

Author: Grafiati
Published: 4 March 2024
Last updated: 31 July 2025

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Journal articles on the topic "DnaB helicase"

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Titok, Marina, Catherine Suski, Bérengère Dalmais, S. Dusko Ehrlich, and Laurent Jannière. "The replicative polymerases PolC and DnaE are required for theta replication of the Bacillus subtilis plasmid pBS72." Microbiology 152, no. 5 (2006): 1471–78. http://dx.doi.org/10.1099/mic.0.28693-0.

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Plasmids are the tools of choice for studying bacterial functions involved in DNA maintenance. Here a genetic study on the replication of a novel, low-copy-number, Bacillus subtilis plasmid, pBS72, is reported. The results show that two plasmid elements, the initiator protein RepA and an iteron-containing origin, and at least nine host-encoded replication proteins, the primosomal proteins DnaB, DnaC, DnaD, DnaG and DnaI, the DNA polymerases DnaE and PolC, and the polymerase cofactors DnaN and DnaX, are required for pBS72 replication. On the contrary, the cellular initiators DnaA and PriA, the
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Hayashi, Chihiro, Erika Miyazaki, Shogo Ozaki, Yoshito Abe, and Tsutomu Katayama. "DnaB helicase is recruited to the replication initiation complex via binding of DnaA domain I to the lateral surface of the DnaB N-terminal domain." Journal of Biological Chemistry 295, no. 32 (2020): 11131–43. http://dx.doi.org/10.1074/jbc.ra120.014235.

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The DNA replication protein DnaA in Escherichia coli constructs higher-order complexes on the origin, oriC, to unwind this region. DnaB helicase is loaded onto unwound oriC via interactions with the DnaC loader and the DnaA complex. The DnaB–DnaC complex is recruited to the DnaA complex via stable binding of DnaB to DnaA domain I. The DnaB–DnaC complex is then directed to unwound oriC via a weak interaction between DnaB and DnaA domain III. Previously, we showed that Phe46 in DnaA domain I binds to DnaB. Here, we searched for the DnaA domain I–binding site in DnaB. The DnaB L160A variant was i
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Bazin, Alexandre, Mickaël Cherrier, and Laurent Terradot. "Structural insights into DNA replication initiation in Helicobacter pylori." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1632. http://dx.doi.org/10.1107/s2053273314083673.

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In Gram-negative bacteria, opening of DNA double strand during replication is performed by the replicative helicase DnaB. This protein allows for replication fork elongation by unwinding DNA and interacting with DnaG primase. DnaB is composed of two domains: an N-terminal domain (NTD) and a C-terminal domain (CTD) connected by a flexible linker. The protein forms two-tiered hexamers composed of a NTD-ring and a CTD-ring. In Escherichia coli, the initiator protein DnaA binds to the origin of replication oriC and induces the opening of a AT-rich region. The replicative helicase DnaB is then load
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Huang, Yen-Hua, and Cheng-Yang Huang. "Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT." BioMed Research International 2014 (2014): 1–14. http://dx.doi.org/10.1155/2014/195162.

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Replication restart primosome is a complex dynamic system that is essential for bacterial survival. This system uses various proteins to reinitiate chromosomal DNA replication to maintain genetic integrity after DNA damage. The replication restart primosome inEscherichia coliis composed of PriA helicase, PriB, PriC, DnaT, DnaC, DnaB helicase, and DnaG primase. The assembly of the protein complexes within the forked DNA responsible for reloading the replicative DnaB helicase anywhere on the chromosome for genome duplication requires the coordination of transient biomolecular interactions. Over
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Sharma, Dhakaram Pangeni, Ramachandran Vijayan, Syed Arif Abdul Rehman, and Samudrala Gourinath. "Structural insights into the interaction of helicase and primase in Mycobacterium tuberculosis." Biochemical Journal 475, no. 21 (2018): 3493–509. http://dx.doi.org/10.1042/bcj20180673.

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The helicase–primase interaction is an essential event in DNA replication and is mediated by the highly variable C-terminal domain of primase (DnaG) and N-terminal domain of helicase (DnaB). To understand the functional conservation despite the low sequence homology of the DnaB-binding domains of DnaGs of eubacteria, we determined the crystal structure of the helicase-binding domain of DnaG from Mycobacterium tuberculosis (MtDnaG-CTD) and did so to a resolution of 1.58 Å. We observed the overall structure of MtDnaG-CTD to consist of two subdomains, the N-terminal globular region (GR) and the C
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Nagata, Koji, Akitoshi Okada, Jun Ohtsuka, et al. "Crystal structure of the complex of the interaction domains of Escherichia coli DnaB helicase and DnaC helicase loader: structural basis implying a distortion-accumulation mechanism for the DnaB ring opening caused by DnaC binding." Journal of Biochemistry 167, no. 1 (2019): 1–14. http://dx.doi.org/10.1093/jb/mvz087.

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Abstract Loading the bacterial replicative helicase DnaB onto DNA requires a specific loader protein, DnaC/DnaI, which creates the loading-competent state by opening the DnaB hexameric ring. To understand the molecular mechanism by which DnaC/DnaI opens the DnaB ring, we solved 3.1-Å co-crystal structure of the interaction domains of Escherichia coli DnaB–DnaC. The structure reveals that one N-terminal domain (NTD) of DnaC interacts with both the linker helix of a DnaB molecule and the C-terminal domain (CTD) of the adjacent DnaB molecule by forming a three α-helix bundle, which fixes the rela
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Donate, L. E., M. Bárcena, O. Llorca, N. Dixon, and J. M. Carazo. "Quaternary Polymorphism in Helicases and the DnaB.DnaC Complex." Microscopy and Microanalysis 6, S2 (2000): 272–73. http://dx.doi.org/10.1017/s1431927600033857.

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Strand separation in double stranded DNA is achieved in vivo by a class of enzymes called helicases in a process fuelled by hydrolysis of nucleoside triphosphates. DnaB is the major replicative helicase in E.coli. For chromosomal replication to initiate, DnaB needs to interact with a partner protein, namely DnaC, which after properly loading DnaB onto the DNA template at the origin of replication is subsequently released from the complex. DnaB turns to be functionally active as a helicase only after DnaC has been released from the complex. The native DnaB is a homohexamer of molecular weight 3
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Saveson, Catherine J., and Susan T. Lovett. "Enhanced Deletion Formation by Aberrant DNA Replication in Escherichia coli." Genetics 146, no. 2 (1997): 457–70. http://dx.doi.org/10.1093/genetics/146.2.457.

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Repeated genes and sequences are prone to genetic rearrangements including deletions. We have investigated deletion formation in Escherichia coli strains mutant for various replication functions. Deletion was selected between 787 base pair tandem repeats carried either on a ColE1-derived plasmid or on the E. coli chromosome. Only mutations in functions associated with DNA Polymerase III elevated deletion rates in our assays. Especially large increases were observed in strains mutant in dnaQ the ϵ editing subunit of Pol III, and dnuB, the replication fork helicase. Mutations in several other fu
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Odegrip, Richard, Stephan Schoen, Elisabeth Haggård-Ljungquist, Kyusung Park, and Dhruba K. Chattoraj. "The Interaction of Bacteriophage P2 B Protein with Escherichia coli DnaB Helicase." Journal of Virology 74, no. 9 (2000): 4057–63. http://dx.doi.org/10.1128/jvi.74.9.4057-4063.2000.

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ABSTRACT Bacteriophage P2 requires several host proteins for lytic replication, including helicase DnaB but not the helicase loader, DnaC. Some genetic studies have suggested that the loading is done by a phage-encoded protein, P2 B. However, a P2 minichromosome containing only the P2 initiator gene A and a marker gene can be established as a plasmid without requiring the P2 B gene. Here we demonstrate that P2 B associates with DnaB. This was done by using the yeast two-hybrid system in vivo and was confirmed in vitro, where 35S-labeled P2 B bound specifically to DnaB adsorbed to Q Sepharose b
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Spinks, Richard R., Lisanne M. Spenkelink, Sarah A. Stratmann, et al. "DnaB helicase dynamics in bacterial DNA replication resolved by single-molecule studies." Nucleic Acids Research 49, no. 12 (2021): 6804–16. http://dx.doi.org/10.1093/nar/gkab493.

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Abstract In Escherichia coli, the DnaB helicase forms the basis for the assembly of the DNA replication complex. The stability of DnaB at the replication fork is likely important for successful replication initiation and progression. Single-molecule experiments have significantly changed the classical model of highly stable replication machines by showing that components exchange with free molecules from the environment. However, due to technical limitations, accurate assessments of DnaB stability in the context of replication are lacking. Using in vitro fluorescence single-molecule imaging, w
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Dissertations / Theses on the topic "DnaB helicase"

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Atkinson, John David. "Regulation of the E. coli Replicative Helicase DnaB by the Helicase Loader DnaC." Thesis, University of Glasgow, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.485809.

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The helicase proteins directly ~esponsible for unwinding chromosomal DNA during DNA replication in bacteria, archaea and eukaryotes adopt a ring-shaped conformation for rapid displacement ofthe parental DNA duplex. As the DNA substrate is engulfed by the helicase during t~slocation, accessory proteins are required for placement ofthe helicase onto the DNA substrate either by breaking the ringed complex, thus allowing DNA to pass into the central channel, or by assembling the helicase around the DNA. In E. coli, the replicative helicase is a hexameric complex of six DnaB monomers, whilst the ac
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Arribas, Bosacoma Raquel. "Resolució de l'estructura tridimensional de l'helicasa hexamètrica DnaB." Doctoral thesis, Universitat de Girona, 2009. http://hdl.handle.net/10803/7639.

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Es presenta el model atòmic a 4.5 Å de DnaB, la principal helicasa replicativa bacteriana, d'Aquifex aeolicus. És un anell hexamèric de 100 Å d'amplada i 80 Å d'alçada amb dues capes de simetria diferenciada, la dels dominis N-terminals en C3 i la dels C-terminals propera a C6. El diàmetre central és de 25 Å al llarg d'ambdues capes, principal diferència amb les estructures prèvies, on era 25 Å més estret a la capa N-terminal. L'estretament s'origina pel trencament d'una de les dues superfícies d'interacció entre monòmers N-terminals, cosa que augmenta la flexibilitat del subdomini implicat. N
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Lo, Allen Tak Yiu. "Protein dynamics on the lagging strand during DNA synthesis." Thesis, School of Chemistry, 2012. https://ro.uow.edu.au/theses/3684.

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DNA replication is one of the vital processes in the cell; it duplicates chromosomal DNA before a cell divides. In all organisms, DNA synthesis on the leading-strand template occurs continuously, whereas on the lagging strand a different mechanism is required. Due to the anti-parallel structure of double-stranded DNA, lagging-strand synthesis requires repeated RNA priming by a specialist primase and synthesis of short Okazaki fragments. How proteins carry out this dynamic process is still unknown. For Escherichia coli DNA replication, a lagging-strand three-point switch was proposed in 1999 to
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Weigelt, Johan. "Development of new NMR techniques and the structure of the N-terminal domain of Escherichia coli DnaB helicase /." Stockholm, 1999. http://diss.kib.ki.se/1999/91-628-3414-2.

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McRobbie, Anne-Marie M. "Splitting, joining and cutting : mechanistic studies of enzymes that manipulate DNA." Thesis, University of St Andrews, 2010. http://hdl.handle.net/10023/951.

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DNA is a reactive and dynamic molecule that is continually damaged by both exogenous and endogenous agents. Various DNA repair pathways have evolved to ensure the faithful replication of the genome. One such pathway, nucleotide excision repair (NER), involves the concerted action of several proteins to repair helix-distorting lesions that arise following exposure to UV light. Mutation of NER proteins is associated with several genetic diseases, including xeroderma pigmentosum that can arise upon mutation of the DNA helicase, XPD. The consequences of introducing human mutations into the gene en
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Song, Daqing. "Homologous Strand Exchange and DNA Helicase Activities in Plant Mitochondria." Diss., CLICK HERE for online access, 2005. http://contentdm.lib.byu.edu/ETD/image/etd931.pdf.

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Rudolf, Jana. "Characterisation of XPD from Sulfolobus acidocaldarius : an iron-sulphur cluster containing DNA repair helicase." Thesis, St Andrews, 2007. http://hdl.handle.net/10023/159.

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Leah, Labib. "Helicase Purification for DNA Sequencing." Thesis, Université d'Ottawa / University of Ottawa, 2014. http://hdl.handle.net/10393/31341.

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BACKGROUND: A method to increase accuracy and ease-of-use, while decreasing time and cost in deoxyribonucleic acid (DNA) sequence identification, is sought after. Helicase, which unwinds DNA, and avidin, which strongly attracts biotin for potential attraction of biotinylated DNA segments, were investigated for use in a novel DNA sequencing method. AIM: This study aimed to (1) purify bacteriophage T7 gene product 4 helicase and helicase-avidin fusion protein in a bacterial host and (2) characterize their functionality. METHODS: Helicase and helicase-avidin were cloned for purification from bact
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Korhonen, Jenny. "Functional and structural characterization of the human mitochondrial helicase /." Stockholm : Karolinska institutet, 2007. http://diss.kib.ki.se/2007/978-91-7357-102-2/.

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Johnson, Vinu. "Structural and Biophysical Studies of Single-Stranded DNA Binding Proteins and dnaB Helicases, Proteins Involved in DNA Replication and Repair." University of Toledo / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1198939056.

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Books on the topic "DnaB helicase"

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D, Knudsen Walter, and Bruns Sam S, eds. Bacterial DNA, DNA polymerase, and DNA helicases. Nova Science, 2009.

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Spies, Maria, ed. DNA Helicases and DNA Motor Proteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-5037-5.

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Lombard, David B. Biochemistry and genetics of recq-helicases. Kluwer Academic Publishers, 2001.

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Lombard, David B. Biochemistry and genetics of recq-helicases. Kluwer Academic Publishers, 2001.

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N, Potaman Vladimir, ed. Triple-helical nucleic acids. Spinger, 1996.

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Helicases: Methods and protocols. Humana Press, 2010.

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Abdelhaleem, Mohamed M. Helicases: Methods and Protocols. Humana Press, 2012.

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Spies, Maria. DNA Helicases and DNA Motor Proteins. Springer London, Limited, 2012.

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Spies, Maria. DNA Helicases and DNA Motor Proteins. Springer New York, 2014.

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Lombard, David B. Biochemistry and Genetics of RecQ-Helicases. Springer, 2012.

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Book chapters on the topic "DnaB helicase"

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Schomburg, Dietmar, and Ida Schomburg. "DNA helicase 3.6.4.12." In Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36260-6_24.

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Kokubo, Tetsuro. "Chromodomain Helicase DNA Binding (CHD)." In Encyclopedia of Systems Biology. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_1619.

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Klein, Hannah L. "DNA helicases in recombination." In Molecular Genetics of Recombination. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71021-9_5.

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Jovin, Thomas M. "The Origin of Left-Handed Poly[d(G-C)]." In Methods in Molecular Biology. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3084-6_1.

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AbstractThe discovery of a reversible transition in the helical sense of a double-helical DNA was initiated by the first synthesis in 1967 of the alternating sequence poly[d(G-C)]. In 1968, exposure to high salt concentration led to a cooperative isomerization of the double helix manifested by an inversion in the CD spectrum in the 240–310 nm range and in an altered absorption spectrum. The tentative interpretation, reported in 1970 and then in detailed form in a 1972 publication by Pohl and Jovin, was that the conventional right-handed B-DNA structure (R) of poly[d(G-C)] transforms at high sa
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Zhang, Suisheng, and Frank Grosse. "Molecular Characterization of Nuclear DNA Helicase II (RNA Helicase A)." In Methods in Molecular Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-355-8_21.

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Lu, Linchao, Weidong Jin, Hao Liu, and Lisa L. Wang. "RECQ DNA Helicases and Osteosarcoma." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-04843-7_7.

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Lu, Linchao, Weidong Jin, and Lisa L. Wang. "RECQ DNA Helicases and Osteosarcoma." In Current Advances in the Science of Osteosarcoma. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-43085-6_3.

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Soultanas, Panos, and Edward Bolt. "Replicative DNA Helicases and Primases." In Molecular Life Sciences. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-6436-5_57-6.

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Soultanas, Panos, and Edward Bolt. "Replicative DNA Helicases and Primases." In Molecular Life Sciences. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4614-1531-2_57.

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Yamakawa, Emeritus Hiromi. "Applications to Circular DNA." In Helical Wormlike Chains in Polymer Solutions. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60817-9_7.

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Conference papers on the topic "DnaB helicase"

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Ha, T., H. P. Babcock, W. Cheng, T. M. Lohman, and S. Chu. "Single molecule fluorescence study of DNA helicase activity." In Conference on Lasers and Electro-Optics (CLEO 2000). Technical Digest. Postconference Edition. TOPS Vol.39. IEEE, 2000. http://dx.doi.org/10.1109/cleo.2000.907430.

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Zhou, Lifeng, Alexander E. Marras, Carlos E. Castro, and Hai-jun Su. "Pseudo-Rigid-Body Models of Compliant DNA Origami Mechanisms." In ASME 2015 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/detc2015-46838.

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In this paper, we introduce the strategy of designing and analyzing compliant nanomechanisms fabricated with DNA origami which we call compliant DNA origami mechanism (CDOM). The rigid, compliant and flexible parts are constructed by a bunch of double-stranded DNA (dsDNA) helices, fewer dsDNA helices and single-stranded DNA (ssDNA) strands respectively. Just like in macroscopic compliant mechanisms, a CDOM generates its motion via deformation of at least one structural member. During the motion, strain energy is stored and released in the mechanism. These CDOM can suppress thermal fluctuations
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Lee, C. H., H. Teng, and J. S. Chen. "Atomistic to Continuum Modeling of DNA Molecules." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13157.

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The mechanical properties of DNA has very important biological implication. For example, the bending and twisting rigidities of DNA affect how it wraps around histones to form chromosomes, bends upon interactions with proteins, supercoils during replication process, and packs into the confined space within a virus. Many biologically important processes involving DNA are accompanied by the deformations of double helical structure of DNA.
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Laughton, C. A., and S. Neidle. "DNA Triple Helices a Molecular Dynamics Study." In Advances in biomolecular simulations. AIP, 1991. http://dx.doi.org/10.1063/1.41360.

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Afifi, Marwa, Breelyn A. Wilky, Catherine Kim, Venu Raman, and David Loeb. "Abstract 4170: The RNA helicase, DDX3, modulates DNA damage repair in Ewing sarcoma." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4170.

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Vanhauwaert, Suzanne, Kaat Durinck, Els Janssens, et al. "Abstract 4886: The BRIP1 DNA helicase is a 17q dosage sensitive cooperative driver in neuroblastoma." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4886.

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Manoj, P., Chang-Ki Min, Taiha Joo, and C. T. Aravindakumar. "Ultrafast Charge Transfer Dynamics of a Modified Double Helical DNA." In International Conference on Ultrafast Phenomena. OSA, 2006. http://dx.doi.org/10.1364/up.2006.thd6.

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Zoppoli, Gabriele, Marie Regairaz, Elisabetta Leo, William C. Reinhold, and Yves Pommier. "Abstract 4693: The putative DNA/RNA Helicase Schlafen-11 sensitizes cancer cells to topoisomerase I inhibitors." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4693.

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Baumstark, Daniela, Sina Berndl, Clemens Wagner, Elke Mayer-Enthart, Janez Barbaric, and Hans-Achim Wagenknecht. "Fluorescent and self-assembled helical chromophore arrays based on DNA architecture." In XIVth Symposium on Chemistry of Nucleic Acid Components. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2008. http://dx.doi.org/10.1135/css200810286.

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Hussain Shah, Syed Imran, Saptarshi Ghosh, and Sungjoon Lim. "A Novel DNA Inspired Mode and Frequency Reconfigurable Origami Helical Antenna." In 2018 IEEE International Symposium on Antennas and Propagation & USNC/URSI National Radio Science Meeting. IEEE, 2018. http://dx.doi.org/10.1109/apusncursinrsm.2018.8608572.

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Reports on the topic "DnaB helicase"

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Bussen, Wendy L. The Roles of the BLM Helicase in Homologous Recombination and DNA Repair. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada436923.

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Beal, P. A., and P. B. Dervan. Recognition of Double Helical DNA by Alternate Strand Triple Helix Formation. Defense Technical Information Center, 1992. http://dx.doi.org/10.21236/ada251499.

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Elbaum, Michael, and Peter J. Christie. Type IV Secretion System of Agrobacterium tumefaciens: Components and Structures. United States Department of Agriculture, 2013. http://dx.doi.org/10.32747/2013.7699848.bard.

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Objectives: The overall goal of the project was to build an ultrastructural model of the Agrobacterium tumefaciens type IV secretion system (T4SS) based on electron microscopy, genetics, and immunolocalization of its components. There were four original aims: Aim 1: Define the contributions of contact-dependent and -independent plant signals to formation of novel morphological changes at the A. tumefaciens polar membrane. Aim 2: Genetic basis for morphological changes at the A. tumefaciens polar membrane. Aim 3: Immuno-localization of VirB proteins Aim 4: Structural definition of the substrate
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